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Protein

Unconventional myosin-X

Gene

MYO10

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.By similarity9 Publications

GO - Molecular functioni

  • actin-dependent ATPase activity Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
  • plus-end directed microfilament motor activity Source: UniProtKB

GO - Biological processi

  • cytoskeleton-dependent intracellular transport Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of filopodium assembly Source: UniProtKB
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Transport

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-X
Alternative name(s):
Unconventional myosin-10
Gene namesi
Name:MYO10
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • filopodium membrane Source: UniProtKB-SubCell
  • filopodium tip Source: UniProtKB
  • lamellipodium Source: MGI
  • myosin complex Source: UniProtKB-KW
  • ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20522052Unconventional myosin-XPRO_0000123472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei963 – 9631PhosphoserineBy similarity
Modified residuei966 – 9661PhosphoserineBy similarity
Modified residuei1152 – 11521PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP79114.
PRIDEiP79114.

Expressioni

Tissue specificityi

Detected in kidney, testis, liver, kidney, cerebellum and brain cortex (at protein level).1 Publication

Interactioni

Subunit structurei

Monomer, when in an inactive confomation in the cytosol. Homodimer in its active, membrane-bound conformation; antiparallel coiled coil-mediated dimer formation. Interacts with ECM29. Interacts with NEO 1. Interacts with VASP. Interacts with DCC and ITGB5; the presence of DCC inhibits ITGB5 binding. Interacts with tubulin; ITGB5 or DCC binding inhibits tubulin binding. Interacts strongly with CALM3 and weakly with CALM, the CALM3 interaction is essential for function in filopodial extension and motility (By similarity). Interacts with ITGB1, ITGB3 and ITGB5.By similarity4 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-46150N.
IntActiP79114. 6 interactions.
STRINGi9913.ENSBTAP00000026812.

Structurei

3D structure databases

ProteinModelPortaliP79114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 739677Myosin motorAdd
BLAST
Domaini742 – 76322IQ 1PROSITE-ProRule annotationAdd
BLAST
Domaini764 – 78724IQ 2PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 81730IQ 3PROSITE-ProRule annotationAdd
BLAST
Domaini1206 – 130499PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini1386 – 1491106PH 2PROSITE-ProRule annotationAdd
BLAST
Domaini1541 – 1689149MyTH4PROSITE-ProRule annotationAdd
BLAST
Domaini1694 – 2038345FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni815 – 90995SAH1 PublicationAdd
BLAST
Regioni884 – 93451Mediates antiparallel dimerizationBy similarityAdd
BLAST

Domaini

Interaction between the motor domain and the tail leads to an inactive, monomeric conformation. Phospholipid binding via the PH domains leads to the formation of the active, dimeric form of the protein and strongly increases actin-dependent ATPase activity and motor activity.
Interacts with membranes containing phosphatidylinositol-3,4,5-trisphosphate via the PH domains.
IQ 3 domain mediates high-affinity calcium-dependent binding to CALM3/CLP.By similarity
The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds. It can refold after extension suggesting an in vivo force-dependent function. The isolated SAH domain is monomeric; however, in its distal part seems to form a semirigid helical structure which overlaps with a region shown to mediate antiparallel coiled coil-mediated dimerization (PubMed:25122759).1 Publication

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 3 IQ domains.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated
Contains 1 MyTH4 domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007044.
HOVERGENiHBG052553.
InParanoidiP79114.
KOiK12559.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 4 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
PF00788. RA. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 4 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P79114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNFFPEGTR VWLRENGQHF PSTVNSCAEG VVVFQTDYGQ VFTYKQSTIT
60 70 80 90 100
HQKVMPMQPT DEEGVDDMAT LTELHGGAIM HNLYQRYKRN QIYTYIGSII
110 120 130 140 150
ASVNPYKTIT GLYSRDAVDR YSRCHLGELP PHVFAIANEC YRCLWKRHDN
160 170 180 190 200
QCVLISGESG AGKTESTKLI LKFLSAISQQ SVDLSSKEKT SSVEQAILES
210 220 230 240 250
SPIMEAFGNA KTVYNNNSSR FGKFVQLNIG QKGNIQGGRI VDYLLEKNRV
260 270 280 290 300
VRQNPGERNY HIFYALLAGL GHEEREEFYL SVPENYHYLN QSGCVTDRTI
310 320 330 340 350
SDQESFREVI MAMEVMQFSK EEVREVLRLL AGILHLGNIE FITAGGAQVS
360 370 380 390 400
FKTALGRSAE LLGLDPAQLT DALTQRSMFL RGEEILTPLN VQQAADSRDS
410 420 430 440 450
LAMALYARCF EWVIKKINSR IKGKDDFKSI GILDIFGFEN FEVNHFEQFN
460 470 480 490 500
INYANEKLQE YFNKHIFSLE QLEYSREGLV WEDIDWIDNG ECLDLIEKKL
510 520 530 540 550
GLLALINEES HFPQATDSTL LEKLHNQHAN NHFYVKPRVA VNNFGVKHYA
560 570 580 590 600
GEVQYDVRGI LEKNRDTFRD DLLNLLRESR FDFIYDLFEH VSSRNNQDTL
610 620 630 640 650
KCGSKHRRPT VSSQFKDSLH SLMATLSASN PFFVRCIKPN MQKMPDQFDQ
660 670 680 690 700
AVVVNQLRYS GMLETVRIRK AGYAVRRPFQ DFYKRYKVLM RNVALPEDIR
710 720 730 740 750
GKCTALLQLY DASNSEWQLG KTKVFLRESL EQKLEKRQEE EVTRAAMVIR
760 770 780 790 800
AHVLGYLARK QYKKVLDCVV IIQKNYRAFL LRRRFLHLKK AAVVFQKQLR
810 820 830 840 850
GQIARRVYRQ LLAEKRAEEE KRKREEEEKR KREEEERERE RERREAELRA
860 870 880 890 900
QQEEAARKQR ELEALQQESQ RAAELSRELE KQKENKQVEE ILRLEKEIED
910 920 930 940 950
LQRMKERQEL SLTEASLQKL QQLRDEELRR LEDEACRAAQ EFLESLNFDE
960 970 980 990 1000
IDECVRNIER SLSVGSGCTG EQGAGAEKPS FNFSQPYPEE EEVDEGFEAD
1010 1020 1030 1040 1050
DDAFKDSPNP SEHGHSDQRT SGIRTSDESS EEDPYMNDTV VPTSPSADST
1060 1070 1080 1090 1100
VLLAPSEHDS SAGEPTYCLP QTPGALPAPE GDYDYDQDDY EDGAITSGSS
1110 1120 1130 1140 1150
VTFSNSCSSQ WSPDYRCSVG TYNSSGAYRF SSEGAQSSFE DSEEDFDSRF
1160 1170 1180 1190 1200
DTDDELSYRR DSVYSCVTLP YFHSFLYMKG GLMNSWKRRW CVLKDETFLW
1210 1220 1230 1240 1250
FRSKQEALKQ GWLHKKGGGS STLSRRNWKK RWFVLRQAKL MYFENDSEEK
1260 1270 1280 1290 1300
LKGTVEVRAA KEIIDNTSKE NGIDIIMADR TFHLIAESPE DASQWFSVLS
1310 1320 1330 1340 1350
QVHASTDQEI REMHDEQANP QNAVGTLDVG LIDSVCASDS PDRPNSFVII
1360 1370 1380 1390 1400
TANRVLHCNA DTPEEMHHWI TLLQRSKGDT RVEGQEFIVR GWLHKEVKNS
1410 1420 1430 1440 1450
PKMSSLKLKK RWFVLTHNSL DYYKSSEKNA LKLGTLVLNS LCSVVPPDEK
1460 1470 1480 1490 1500
IFKETGYWNV TVYGRKHCYR LYTKLLNEAT RWSSAIQNVT DTKAPIDTPT
1510 1520 1530 1540 1550
QQLIQDIKEN CLNSDVVEQI YKRNPILRHT HHPLHSPLLP LPYGDINLNL
1560 1570 1580 1590 1600
LKDKGYTTLQ DEAIKIFNSL QQLESMSDPI PIIQGILQTG HDLRPLRDEL
1610 1620 1630 1640 1650
YCQLIKQTNK VPHPGSVGNL CSWQILTCLS CTFLPSRGIL KYLKFHLRRI
1660 1670 1680 1690 1700
REQFPGTEME KYALFIYESL KKTKCREFVP SRDEIEALIH RQEMTSTVHC
1710 1720 1730 1740 1750
HGGGSCKITV NSHTTAGEVV EKLIRGLAME DSRNMFALFE YNGHVDKAIE
1760 1770 1780 1790 1800
SRTIVADVLA KFEKLAATSE VGEQPWKFYF KLYCFLDTDN VPKDSVEFAF
1810 1820 1830 1840 1850
MFEQAHEAVI HGHYPAPEEN LQVLAALRLQ YLQGDYAPHA PVPPLEEVYS
1860 1870 1880 1890 1900
LQRLKARISQ STKSFTPGER LEKRRTSFLE GTLRRSFRTG SAIRQKAEEE
1910 1920 1930 1940 1950
QMVDMWVKEE VCSARASILD KWKKFQGMSQ EQAMAKYMAL IKEWPGYGST
1960 1970 1980 1990 2000
LFDVECKEGG FPQDLWLGVS ADAVSVYKRG EGRPLEVFQY EHILSFGAPL
2010 2020 2030 2040 2050
ANTYKIVVDE RELLFETSEV VDVAKLMKAY ISMIVKKRYS TSRSVSSQGS

SR
Length:2,052
Mass (Da):235,839
Last modified:May 1, 1997 - v1
Checksum:i43DF13424B4B2D28
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55042 mRNA. Translation: AAB39486.1.
PIRiT18519.
RefSeqiNP_776819.1. NM_174394.2.
UniGeneiBt.103339.

Genome annotation databases

GeneIDi281935.
KEGGibta:281935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55042 mRNA. Translation: AAB39486.1.
PIRiT18519.
RefSeqiNP_776819.1. NM_174394.2.
UniGeneiBt.103339.

3D structure databases

ProteinModelPortaliP79114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46150N.
IntActiP79114. 6 interactions.
STRINGi9913.ENSBTAP00000026812.

Proteomic databases

PaxDbiP79114.
PRIDEiP79114.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281935.
KEGGibta:281935.

Organism-specific databases

CTDi4651.

Phylogenomic databases

eggNOGiKOG4229. Eukaryota.
COG5022. LUCA.
HOGENOMiHOG000007044.
HOVERGENiHBG052553.
InParanoidiP79114.
KOiK12559.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 4 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR031971. MYO10_CC.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000159. RA_dom.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF16735. MYO10_CC. 1 hit.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 1 hit.
PF00169. PH. 2 hits.
PF00788. RA. 1 hit.
[Graphical view]
PRINTSiPR00193. MYOSINHEAVY.
SMARTiSM00295. B41. 1 hit.
SM00015. IQ. 3 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 1 hit.
SM00233. PH. 2 hits.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 2 hits.
SSF50729. SSF50729. 4 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50057. FERM_3. 1 hit.
PS50096. IQ. 2 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51016. MYTH4. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Myosin-X, a novel myosin with pleckstrin homology domains, associates with regions of dynamic actin."
    Berg J.S., Derfler B.H., Pennisi C.M., Corey D.P., Cheney R.E.
    J. Cell Sci. 113:3439-3451(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Aorta.
  2. Cited for: FUNCTION, INTERACTION WITH CALM.
  3. "Myosin-X is an unconventional myosin that undergoes intrafilopodial motility."
    Berg J.S., Cheney R.E.
    Nat. Cell Biol. 4:246-250(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Myosin-X provides a motor-based link between integrins and the cytoskeleton."
    Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S.
    Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITGB1; ITGB3 AND ITGB5.
  5. "Mechanism of action of myosin X, a membrane-associated molecular motor."
    Kovacs M., Wang F., Sellers J.R.
    J. Biol. Chem. 280:15071-15083(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIN BINDING AND ATP HYDROLYSIS.
  6. "Myosin-X is a molecular motor that functions in filopodia formation."
    Bohil A.B., Robertson B.W., Cheney R.E.
    Proc. Natl. Acad. Sci. U.S.A. 103:12411-12416(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF FILOPODIA ASSEMBLY AND REGULATION OF CELL SHAPE.
  7. "Myosin X regulates sealing zone patterning in osteoclasts through linkage of podosomes and microtubules."
    McMichael B.K., Cheney R.E., Lee B.S.
    J. Biol. Chem. 285:9506-9515(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Myosin-X induces filopodia by multiple elongation mechanism."
    Watanabe T.M., Tokuo H., Gonda K., Higuchi H., Ikebe M.
    J. Biol. Chem. 285:19605-19614(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "PtdIns(3,4,5)P is a regulator of myosin-X localization and filopodia formation."
    Plantard L., Arjonen A., Lock J.G., Nurani G., Ivaska J., Stromblad S.
    J. Cell Sci. 123:3525-3534(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, PHOSPHATIDYLINOSITOL-3,4,5-TRISPHOSPHATE BINDING.
  10. "Single-molecule stepping and structural dynamics of myosin X."
    Sun Y., Sato O., Ruhnow F., Arsenault M.E., Ikebe M., Goldman Y.E.
    Nat. Struct. Mol. Biol. 17:485-491(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALM.
  11. "Phospholipid-dependent regulation of the motor activity of myosin X."
    Umeki N., Jung H.S., Sakai T., Sato O., Ikebe R., Ikebe M.
    Nat. Struct. Mol. Biol. 18:783-788(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH CALM, SUBUNIT.
  12. "Stable single alpha-helices are constant force springs in proteins."
    Wolny M., Batchelor M., Knight P.J., Paci E., Dougan L., Peckham M.
    J. Biol. Chem. 289:27825-27835(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SAH DOMAIN.

Entry informationi

Entry nameiMYO10_BOVIN
AccessioniPrimary (citable) accession number: P79114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-10 (MYH10).Curated
Originally predicted to contain a coiled coil domain but shown to contain a stable SAH domain instead.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.